About: Protein Kinase C subtype δ interacts with Venezuelan equine encephalitis virus capsid protein and regulates viral RNA binding through modulation of capsid phosphorylation

Facets (new session)
Description
Metadata
Settings
- owl:sameAs
- Inference Rule:

About: Protein Kinase C subtype δ interacts with Venezuelan equine encephalitis virus capsid protein and regulates viral RNA binding through modulation of capsid phosphorylation Goto Sponge NotDistinct Permalink

An Entity of Type : schema:ScholarlyArticle, within Data Space : wasabi.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	Protein Kinase C subtype δ interacts with Venezuelan equine encephalitis virus capsid protein and regulates viral RNA binding through modulation of capsid phosphorylation
Creator	Lin, Shih-Chao Dahal, Bibha Akhrymuk, Ivan Lehman, Caitlin Carey, Brian Bracci, Nicole Finstuen-Magro, Sarah Id, Kylene Kehn-Hall Pinkham Id, Chelsea Sokoloski Id, Kevin
topic	covid:91e5052a1a7840b87e40f4f199262e4ba50987ae#this
Source	Medline; PMC
abstract	Protein phosphorylation plays an important role during the life cycle of many viruses. Venezuelan equine encephalitis virus (VEEV) capsid protein has recently been shown to be phosphorylated at four residues. Here those studies are extended to determine the kinase responsible for phosphorylation and the importance of capsid phosphorylation during the viral life cycle. Phosphorylation site prediction software suggests that Protein Kinase C (PKC) is responsible for phosphorylation of VEEV capsid. VEEV capsid co-immunoprecipitated with PKCδ, but not other PKC isoforms and siRNA knockdown of PKCδ caused a decrease in viral replication. Furthermore, knockdown of PKCδ by siRNA decreased capsid phosphorylation. A virus with capsid phosphorylation sites mutated to alanine (VEEV CPD) displayed a lower genomic copy to pfu ratio than the parental virus; suggesting more efficient viral assembly and more infectious particles being released. RNA:capsid binding was significantly increased in the mutant virus, confirming these results. Finally, VEEV CPD is attenuated in a mouse model of infection, with mice showing increased survival and decreased clinical signs as compared to mice infected with the parental virus. Collectively our data support a model in which PKCδ mediated capsid phosphorylation regulates viral RNA binding and assembly, significantly impacting viral pathogenesis.
has issue date	2020-03-09(xsd:dateTime)
bibo:doi	10.1371/journal.ppat.1008282
bibo:pmid	32150585
has license	cc-by
sha1sum (hex)	91e5052a1a7840b87e40f4f199262e4ba50987ae
schema:url	https://doi.org/10.1371/journal.ppat.1008282
resource representing a document's title	Protein Kinase C subtype δ interacts with Venezuelan equine encephalitis virus capsid protein and regulates viral RNA binding through modulation of capsid phosphorylation
has PubMed Central identifier	PMC7082041
has PubMed identifier	32150585
schema:publication	PLoS Pathog
resource representing a document's body	covid:91e5052a1a7840b87e40f4f199262e4ba50987ae#body_text
is http://vocab.deri.ie/void#inDataset of	proxy:http/ns.inria.fr/covid19/91e5052a1a7840b87e40f4f199262e4ba50987ae https://covidontheweb.inria.fr:4443/about/id/http/ns.inria.fr/covid19/91e5052a1a7840b87e40f4f199262e4ba50987ae
is schema:about of	named entity 'VIRAL RNA' named entity 'mediated' named entity 'infected' named entity 'plays' named entity 'capsid' named entity 'mutated' named entity 'phosphorylation' named entity 'phosphorylation' named entity 'viral' named entity 'site' named entity 'virus' named entity 'PHOSPHORYLATION' covid:arg/91e5052a1a7840b87e40f4f199262e4ba50987ae named entity 'ISOFORMS' named entity 'RELEASED' named entity 'RNA' named entity 'CONFIRMING' named entity 'PARTICLES' named entity 'COMPARED' named entity 'SIRNA' named entity 'STUDIES' named entity 'SUPPORT' named entity 'KINASE' named entity 'VIRAL REPLICATION' named entity 'VIRAL RNA' named entity 'GENOMIC' named entity 'PHOSPHORYLATION SITE PREDICTION' named entity 'VIRAL PATHOGENESIS' named entity 'ASSEMBLY' named entity 'LIFE CYCLE' named entity 'PHOSPHORYLATION' named entity 'ROLE' named entity 'VIRAL ASSEMBLY' named entity 'COPY' named entity 'PFU' named entity 'RATIO' named entity 'INCREASED' named entity 'BEING' named entity 'CAPSID' named entity 'BUT' named entity 'RNA BINDING' named entity 'A MOUSE' named entity 'HERE' named entity 'MOUSE MODEL' named entity 'RESULTS' named entity 'INFECTION' named entity 'THESE' named entity 'IMPORTANT' named entity 'ALANINE' named entity 'VIRUS' named entity 'RESPONSIBLE' named entity 'DISPLAYED' named entity 'MODEL' named entity 'DATA' named entity 'MODULATION' named entity 'PROTEIN KINASE C' named entity 'PROTEIN PHOSPHORYLATION' named entity 'PHOSPHORYLATION SITES' named entity 'DECREASE' named entity 'EXTENDED' named entity 'ATTENUATED' named entity 'CAPSID PROTEIN' named entity 'MUTATED' named entity 'VENEZUELAN EQUINE ENCEPHALITIS VIRUS' named entity 'DECREASED' named entity 'CAPSID' named entity 'PROTEIN ' named entity 'LOWER' named entity 'CPD'

Faceted Search & Find service v1.13.91 as of Mar 24 2020

Alternative Linked Data Documents: Sponger | ODE Content Formats:

RDF

ODATA

Microdata

About

OpenLink Virtuoso version 07.20.3229 as of Jul 10 2020, on Linux (x86_64-pc-linux-gnu), Single-Server Edition (94 GB total memory)
Data on this page belongs to its respective rights holders.
Virtuoso Faceted Browser Copyright © 2009-2024 OpenLink Software